ArticleProceedings of the National Academy of Sciences of the United States of America2016
Insights into the molecular basis for substrate binding and specificity of the wild-type L-arginine/agmatine antiporter AdiC.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 80 citations in OpenAlex.
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- Chemiosmotic nutrient transport in synthetic cells powered by electrogenic antiport coupled to decarboxylation.Nature communications · 2024Article
- Structure and mechanisms of transport of human Asc1/CD98hc amino acid transporter.Nature communications · 2024Article
- Lactose Permease Scrambles Phospholipids.Biology · 2023Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
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- Insights into the Transport Cycle of LAT1 and Interaction with the Inhibitor JPH203.International journal of molecular sciences · 2023Article
- Describing inhibitor specificity for the amino acid transporter LAT1 from metainference simulations.Biophysical journal · 2022Article
- Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- CaNature communications · 2022Article
- Heteromeric Amino Acid Transporters in Brain: from Physiology to Pathology.Neurochemical research · 2022Review
- Molecular basis for redox control by the human cystine/glutamate antiporter system xcNature communications · 2021Article
- Chemical Approaches for Studying the Biology and Pharmacology of Membrane Transporters: The Histidine/Large Amino Acid Transporter SLC7A5 as a Benchmark.Molecules (Basel, Switzerland) · 2021Review
- The making of a potent L-lactate transport inhibitor.Communications chemistry · 2021Article
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- Rush Hour of LATs towards Their Transport Cycle.Membranes · 2021Review
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- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Comparative Review of the Responses ofGenes · 2020Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pathogenic enterobacteria need to survive the extreme acidity of the stomach to successfully colonize the human gut. Enteric bacteria circumvent the gastric acid barrier by activating extreme acid-resistance responses, such as the arginine-dependent acid resistance system. In this response, l-arginine is decarboxylated to agmatine, thereby consuming one proton from the cytoplasm. In Escherichia coli, the l-arginine/agmatine antiporter AdiC facilitates the export of agmatine in exchange of l-arginine, thus providing substrates for further removal of protons from the cytoplasm and balancing the intracellular pH. We have solved the crystal structures of wild-type AdiC in the presence and absence of the substrate agmatine at 2.6-Å and 2.2-Å resolution, respectively. The high-resolution structures made possible the identification of crucial water molecules in the substrate-binding sites, unveiling their functional roles for agmatine release and structure stabilization, which was further corroborated by molecular dynamics simulations. Structural analysis combined with site-directed mutagenesis and the scintillation proximity radioligand binding assay improved our understanding of substrate binding and specificity of the wild-type l-arginine/agmatine antiporter AdiC. Finally, we present a potential mechanism for conformational changes of the AdiC transport cycle involved in the release of agmatine into the periplasmic space of E. coli.
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